| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PML |
| Uniprot No | P29590 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 59-239aa |
| 氨基酸序列 | QCQAEAKCPKLLPCLHTLCSGCLEASGMQCPICQAPWPLGADTPALDNVFFESLQRRLSVYRQIVDAQAVCTRCKESADFWCFECEQLLCAKCFEAHQWFLKHEARPLAELRNQSVREFLDGTRKTNNIFCSNPNHRTPTLTSIYCRGCSKPLCCSCALLDSSHSELKCDISAEIQQRQEE |
| 预测分子量 | 26.4 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于PML重组蛋白的3篇代表性文献示例(注：部分内容基于领域内经典研究模拟，建议通过学术数据库核实具体信息)：
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1. **文献名称**：*"Structural dissection of PML protein reveals regulatory motifs essential for oncogenic transformation and aggregate formation"*
**作者**：Shen, T.H., de Thé, H., & Lallemand-Breitenbach, V.
**摘要**：通过重组表达人源PML蛋白，解析其B-box和卷曲螺旋结构域的晶体结构，揭示了PML通过多聚化形成核体(PML-NB)的分子机制，并发现砷剂可诱导其构象变化，破坏核体结构，从而抑制白血病发生。
2. **文献名称**：*"Reconstitution of the interferon-γ response in PML-deficient cells by recombinant PML isoforms"*
**作者**：Chelbi-Alix, M.K., & Pelicano, L.
**摘要**：研究利用重组PML异构体(如PML-I和PML-IV)在PML敲除细胞中恢复干扰素-γ信号通路，证实PML通过招募STAT3等转录因子调控抗肿瘤免疫反应，不同异构体功能具有特异性。
3. **文献名称**：*"SUMO modification of recombinant PML regulates its antiviral activity against herpes simplex virus 1"*
**作者**：Everett, R.D., & Chelbi-Alix, M.K.
**摘要**：通过体外表达SUMO化修饰的重组PML蛋白，证明其与病毒蛋白ICP0的相互作用可抑制单纯疱疹病毒复制，揭示了PML核体的SUMO依赖的抗病毒机制。
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**备注**：上述文献为示例性质，实际引用时建议通过PubMed或Web of Science检索最新研究(如关键词“recombinant PML protein SUMO”或“PML-NB in vitro assembly”)，并优先选择高影响力期刊(如*Nature Cell Biology*、*Cell Research*)上的论文。
PML (Promyelocytic Leukemia) protein is a multifunctional regulator implicated in diverse cellular processes, including apoptosis, senescence, antiviral defense, and genome stability. It is a key component of PML nuclear bodies (PML-NBs), dynamic subnuclear structures that orchestrate protein interactions and post-translational modifications. Structurally, PML belongs to the tripartite motif (TRIM) family, characterized by a N-terminal RING domain, two B-box motifs, and a coiled-coil region, which mediate homo-oligomerization and scaffold functions. Alternative splicing generates multiple PML isoforms with distinct C-terminal domains, enabling functional diversity.
The PML gene gained prominence due to its involvement in acute promyelocytic leukemia (APL), where a chromosomal translocation t(15;17) fuses PML with the retinoic acid receptor alpha (RARα). The resulting PML-RARα oncoprotein disrupts normal myeloid differentiation and apoptosis by recruiting transcriptional repressors and disassembling PML-NBs. This discovery directly informed therapeutic breakthroughs: all-trans retinoic acid (ATRA) and arsenic trioxide synergistically degrade PML-RARα while restoring PML-NB function, curing >90% of APL cases.
Recombinant PML proteins, produced via bacterial or mammalian expression systems, are vital tools for studying PML-NB biogenesis, protein interactions (e.g., with p53. DAXX, or Sp100), and post-translational modifications (e.g., SUMOylation, phosphorylation). They enable structural analyses, such as crystallography of the RING-B-box-coiled-coil core, and functional assays probing PML's roles in stress responses, antiviral signaling, and tumor suppression. Engineered PML variants (e.g., SUMO-binding mutants) help dissect mechanisms underlying PML-mediated transcriptional regulation or protein sequestration.
Current research leverages recombinant PML to explore its emerging roles in metabolic regulation, DNA repair, and immune signaling, highlighting its therapeutic potential beyond oncology. Challenges remain in understanding isoform-specific functions and PML-NB plasticity, areas where tailored recombinant constructs continue to provide critical insights.
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